Evidence map›Paper›PMID 26655737›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for specificity and promiscuity in a carrier protein/enzyme system from the sulfur cycle.

Daniel B Grabarczyk, Paul E Chappell, Steven Johnson, Lukas S Stelzl, Susan M Lea, Ben C Berks

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.6field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. In the AlphaproteobacteriumAntioxidants (Basel, Switzerland) · 2023
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Methodologies for "Wiring" Redox Proteins/Enzymes to Electrode Surfaces.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018
    Review
  11. Sulfur Oxidation in the Acidophilic AutotrophicFrontiers in microbiology · 2018
    Review
  12. Article
  13. Sulfur Metabolism ofFrontiers in microbiology · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Daniel B GrabarczykDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;
Paul E ChappellSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Steven JohnsonSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Lukas S StelzlDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom;
Susan M LeaSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.ORCID http://orcid.org/0000-0001-9287-8053
Ben C BerksDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom; ben.berks@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0900888
6 · The paper itself

Abstract

The bacterial Sox (sulfur oxidation) pathway is an important route for the oxidation of inorganic sulfur compounds. Intermediates in the Sox pathway are covalently attached to the heterodimeric carrier protein SoxYZ through conjugation to a cysteine on a protein swinging arm. We have investigated how the carrier protein shuttles intermediates between the enzymes of the Sox pathway using the interaction between SoxYZ and the enzyme SoxB as our model. The carrier protein and enzyme interact only weakly, but we have trapped their complex by using a "suicide enzyme" strategy in which an engineered cysteine in the SoxB active site forms a disulfide bond with the incoming carrier arm cysteine. The structure of this trapped complex, together with calorimetric data, identifies sites of protein-protein interaction both at the entrance to the enzyme active site tunnel and at a second, distal, site. We find that the enzyme distinguishes between the substrate and product forms of the carrier protein through differences in their interaction kinetics and deduce that this behavior arises from substrate-specific stabilization of a conformational change in the enzyme active site. Our analysis also suggests how the carrier arm-bound substrate group is able to outcompete the adjacent C-terminal carboxylate of the carrier arm for binding to the active site metal ions. We infer that similar principles underlie carrier protein interactions with other enzymes of the Sox pathway.

Indexed as

Bacterial ProteinsCatalytic DomainModels, BiologicalModels, ChemicalModels, MolecularOxidation-ReductionOxidoreductases Acting on Sulfur Group DonorsProtein BindingProtein Structure, TertiaryStructure-Activity RelationshipSubstrate SpecificitySulfurThermodynamicsThiosulfatesBacterial ProteinsOxidoreductases Acting on Sulfur Group DonorsSoxZ protein, Paracoccus pantotrophusSulfurThiosulfatesSox systemswinging armthiosulfate oxidation

Identifiers

PMID26655737
PMCPMC4702959
OpenAlexW2180187791

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.